1. Functional cooperation of α-synuclein and VAMP2 in synaptic vesicle recycling
- Author
-
Huan Bao, Edwin R. Chapman, Jichao Sun, Utpal Das, Lina Wang, Sanjay Premi, and Subhojit Roy
- Subjects
0301 basic medicine ,Parkinson's disease ,Vesicle-Associated Membrane Protein 2 ,animal diseases ,Neurotransmission ,Synaptic vesicle ,Synaptic Transmission ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,medicine ,alpha synuclein ,Synaptic vesicle recycling ,Humans ,heterocyclic compounds ,Neurotransmitter ,Alpha-synuclein ,Neurons ,Multidisciplinary ,VAMP2 ,Chemistry ,Biological Transport ,Biological Sciences ,medicine.disease ,nervous system diseases ,030104 developmental biology ,nervous system ,health occupations ,alpha-Synuclein ,Parkinson’s disease ,Synaptic Vesicles ,SNARE Proteins ,Neuroscience ,030217 neurology & neurosurgery ,Function (biology) - Abstract
The function of α-synuclein (α-syn) has been long debated, and two seemingly divergent views have emerged. In one, α-syn binds to VAMP2, acting as a SNARE chaperone—but with no effect on neurotransmission—while another posits that α-syn attenuates neurotransmitter release by restricting synaptic vesicle mobilization and recycling. Here, we show that α-syn–VAMP2 interactions are necessary for α-syn–induced synaptic attenuation. Our data connect divergent views and suggest a unified model of α-syn function.
- Published
- 2019